ID A0A0F2C602_9MICO Unreviewed; 334 AA.
AC A0A0F2C602;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Deacetoxycephalosporin C hydroxylase {ECO:0000313|EMBL:KJQ53095.1};
DE EC=1.14.11.26 {ECO:0000313|EMBL:KJQ53095.1};
GN Name=cefF {ECO:0000313|EMBL:KJQ53095.1};
GN ORFNames=RS85_03176 {ECO:0000313|EMBL:KJQ53095.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ53095.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ53095.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ53095.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJQ53095.1}.
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DR EMBL; JXRU01000038; KJQ53095.1; -; Genomic_DNA.
DR RefSeq; WP_046014404.1; NZ_JXRU01000038.1.
DR AlphaFoldDB; A0A0F2C602; -.
DR STRING; 1263625.RS85_03176; -.
DR PATRIC; fig|1263625.4.peg.3189; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000033425; Unassembled WGS sequence.
DR GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PRINTS; PR00682; IPNSYNTHASE.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682,
KW ECO:0000313|EMBL:KJQ53095.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT DOMAIN 170..272
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 334 AA; 36537 MW; D771A6B5A71D7AF1 CRC64;
MAELSLPILD LSQLDEGLDA AARFRDDLRA ATHDVGFFYL TGTGISPELE ARLHRAALDF
FALPEADKLA IENVNSPHFR GYTRVGGERT QGKVDWREQI DIGPEREPVE EGPAFNRLIG
PNLWPSAQPE LQDVVAEWHA TLSEVARKLL RAWAQTLGAD ETYFDDHFGE PSTLIKIVRY
PGSTEPEPQQ GVGAHKDSGV LTLLWVEPGK GGLQVERDGS WVDAPPVPGA FVVNIGELLE
YATGGYLKAT NHRVVSPKAP DERISIPFFF NPALDKRLPL IELPAELAAE ANGVTEDPNN
PIHALYGENA LKSRLRAHPD VAAIHHADLV GAPV
//